The cell division cycle is one of the most fundamental processes in biology which ensures the controlled proliferation of cells in multicellular organisms. Under normal growth conditions, cell proliferation is tightly regulated in response to diverse intracellular and extracellular signals. This is achieved by a complex network of proto-oncogenes and tumor-suppressor genes that are components of various signal transduction pathways. Activation of a proto-oncogene and/or a loss of a minor suppressor gene can lead to the unregulated activity of the cell cycle machinery. This, in turn, will lead to unregulated cell proliferation and to the accumulation of genetic errors which ultimately result in the development of cancer (Pardee, A. B., Science, 1989, 246:603–608). In the eukaryotic cell cycle a key role is played by the cyclin dependent kinases. CDK complexes are formed via the association of a regulatory cyclin subunit and a catalytic kinase subunit. In mammalian cells, the combination of the kinase subunits (such as CDK1, CDK2, CDK4 or CDK6) with a variety of cyclin subunits (such as cyclin A, B, D1, D2, D3 or E) results in the assembly of functionally distinct kinase complexes. The coordinated activation of these complexes drives the cells through the cell cycle and ensures the fidelity of the process (Draetta, G., Trends Biochem. Sci., 1990, 15:378–382; Sherr, C. J., Cell, 1993, 73:1059–1065). Each step in the cell cycle is regulated by a distinct and specific cyclin-dependent kinase. Regulation occurs at the boundaries of the G1/S and G2/M phases, two major transition points of the cell cycle. For example, complexes of CDK4 and D-type cyclins govern the early G1 phase of the cell cycle, while the activity of the CDK2/cyclin E complex is rate limiting for the G1 to S-phase transition. The CDK2/cyclin A kinase is required for the progression through S-phase and the CDK1/cyclin B complex controls the entry into M-phase (Sherr, 1993). A key regulator of these transitions is CDK1 kinase, a universal intracellular factor which triggers the G2/M transition of the cell cycle in all organisms. Both biochemical and genetic evidence have shown that CDK1 is the primary activity required for a cell to enter mitosis in all eukaryotic cells. In late G2, it is present as an inactive complex of CDK1 and cyclin B. In M phase, it is activated and thereafter displays kinase activity. CDK1 is known to phosphorylate a number of proteins including histone H1, DNA polymerase alpha, RNA polymerase II, retinoblastoma tumor suppressor protein (RB), p53, nucleolin, cAbl and lamin A. The kinase activity of CDK1 is required for entry of cells into mitosis, i.e., for passage from the G2 phase of the cell cycle into the M phase (Lee M. and Nurse P., Trends Genet., 1988, 4:289–90; Dunphy W. G., Brizuela L., Beach D. and Newport J., Cell, 1988, 54:423–431; Gautier J., Norbury C., Lohka M., Nurse P. and Maller J., Cell, 1988, 54:433–439; Cross F., Roberts J. and Weintraub H., Ann. Rev. Cell Biol., 1989, 5:341–395; Hunt, T. and Sherr, C., Curr. Opinion Cell Biol., 1989, 1:268–274; and, Nurse, P., Nature, 1990, 344:503–508). Therefore, using cyclin dependent kinase inhibitors for tumor therapy is believed to inhibit tumor growth or controlling unregulated cell proliferation. Patent application WO 01/25220 describes a series of triazines that bind to ATP or GTP and/or catalyze phosphoryl transfer.